Tuba: Difference between revisions
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<StructureSection load='4cc2' size='340' side='right' caption='Human Tuba 6th SH3 domain complex with N-WASP peptide, glycerol and Cl- ion (PDB code [[4cc2]])' scene=''> | |||
== Function == | |||
'''Tuba''' or '''dynamin-binding protein''' is a scaffold protein found in brain synapses which brings together dynamin and actin regulatory proteins. The N-terminal SH3 domains bind dynamin and the C-terminal SH3 domain binds actin regulatory proteins<ref>PMID:14506234</ref>. | |||
== Disease == | == Disease == | ||
Tuba deficiency causes and abnormal renal ciliary and morphogenetic phenotype. Tuba has a critical role in ciliogenesis and nephrogenesis by regulating Cdc42 activity<ref>PMID:26895965</ref>. | |||
== Relevance == | == Relevance == | ||
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== Structural highlights == | == Structural highlights == | ||
Tuba contains 6 SH3 domains. The C-terminal 6th domain binds proline-rich regions of human actin regulating proteins such as N-WASP and Mena. The peptide forms a polyproline type II helix. The interactions of Tuba with the peptide is via SH3-conserved residues<ref>PMID:24332715</ref>. | Tuba contains 6 SH3 domains. The C-terminal 6th SH3 domain binds proline-rich regions of human actin regulating proteins such as N-WASP and Mena. The peptide forms a polyproline type II helix. The interactions of Tuba with the peptide is via SH3-conserved residues<ref>PMID:24332715</ref>. | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 13:55, 11 February 2019
FunctionTuba or dynamin-binding protein is a scaffold protein found in brain synapses which brings together dynamin and actin regulatory proteins. The N-terminal SH3 domains bind dynamin and the C-terminal SH3 domain binds actin regulatory proteins[1]. DiseaseTuba deficiency causes and abnormal renal ciliary and morphogenetic phenotype. Tuba has a critical role in ciliogenesis and nephrogenesis by regulating Cdc42 activity[2]. RelevanceStructural highlightsTuba contains 6 SH3 domains. The C-terminal 6th SH3 domain binds proline-rich regions of human actin regulating proteins such as N-WASP and Mena. The peptide forms a polyproline type II helix. The interactions of Tuba with the peptide is via SH3-conserved residues[3].
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ReferencesReferences
- ↑ Salazar MA, Kwiatkowski AV, Pellegrini L, Cestra G, Butler MH, Rossman KL, Serna DM, Sondek J, Gertler FB, De Camilli P. Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology domains, links dynamin to regulation of the actin cytoskeleton. J Biol Chem. 2003 Dec 5;278(49):49031-43. Epub 2003 Sep 22. PMID:14506234 doi:http://dx.doi.org/10.1074/jbc.M308104200
- ↑ Baek JI, Kwon SH, Zuo X, Choi SY, Kim SH, Lipschutz JH. Dynamin Binding Protein (Tuba) Deficiency Inhibits Ciliogenesis and Nephrogenesis in Vitro and in Vivo. J Biol Chem. 2016 Apr 15;291(16):8632-43. doi: 10.1074/jbc.M115.688663. Epub 2016, Feb 19. PMID:26895965 doi:http://dx.doi.org/10.1074/jbc.M115.688663
- ↑ Polle L, Rigano LA, Julian R, Ireton K, Schubert WD. Structural Details of Human Tuba Recruitment by InlC of Listeria monocytogenes Elucidate Bacterial Cell-Cell Spreading. Structure. 2013 Dec 10. pii: S0969-2126(13)00429-2. doi:, 10.1016/j.str.2013.10.017. PMID:24332715 doi:http://dx.doi.org/10.1016/j.str.2013.10.017